ID A0A0M1JGB8_9GAMM Unreviewed; 448 AA.
AC A0A0M1JGB8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:KOR31907.1};
GN ORFNames=TI05_10605 {ECO:0000313|EMBL:KOR31907.1};
OS Achromatium sp. WMS3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Achromatium.
OX NCBI_TaxID=1604836 {ECO:0000313|EMBL:KOR31907.1, ECO:0000313|Proteomes:UP000036918};
RN [1] {ECO:0000313|EMBL:KOR31907.1, ECO:0000313|Proteomes:UP000036918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS3 {ECO:0000313|EMBL:KOR31907.1};
RX PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT "Metabolic diversity and ecological niches of Achromatium populations
RT revealed with single-cell genomic sequencing.";
RL Front. Microbiol. 6:822-822(2015).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOR31907.1}.
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DR EMBL; JXSO01000232; KOR31907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M1JGB8; -.
DR PATRIC; fig|1604836.3.peg.1623; -.
DR Proteomes; UP000036918; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KOR31907.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KOR31907.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036918};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..192
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 203..379
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 448 AA; 49145 MW; 7C0BD87914B503C7 CRC64;
MCDYAKASHL YDLSLRKLIG LILLAVNLWI IPSAWAIPKI QSWNTPNGTK VLFVSAPELP
MLDVRVVFNA GSAREAKPGV ALLTNSLLTQ GAGQWDVEQI AERLEAVGVT LSTGSLRDMS
WLSLRTLIMQ PALNTALETL TAILGKPLFT AKDLKRLRNT MLVALNQEEQ KPGTMGTRAL
YKAIYGNHPY ANYPTGTKEA VASINRTDIQ GHYNKYYVAK NAIIALVGAI DRKQAEQIAT
QITSGLTTGA TPPKLPKVPK LDRNQLELLD FPITQSHIYI GQPCITRNDP DYFPLYVGNH
ILGGSGLVSL LSKEIRERRG LSYSVSSALR PMQQQGPFIM GLQTKNSQAK QALGLLMQIL
QRFVQTGPSA VELDAAKRNI TGSFPLGIAS NSAIAEYLSM IGFYNYPLDY LDTFIAKINA
VTAEQIKAAF QRHIHPKHLV TVIVGPVQ
//
